Evidence map›Paper›PMID 21844229›Full record

ArticleInfection and immunity2011

The novel leptospiral surface adhesin Lsa20 binds laminin and human plasminogen and is probably expressed during infection.

Renata Siqueira Mendes, Marina Von Atzingen, Zenaide Maria de Morais, Amane Paldes Gonçales, Solange M T Serrano, Amanda F Asega, Eliete Caló Romero, Silvio Arruda Vasconcellos, Ana Lucia Tabet O Nascimento

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
6.3field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
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  5. Review
  6. A Review on Host-Frontiers in cellular and infection microbiology · 2021
    Review
  7. Article
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  9. Complement Evasion by PathogenicFrontiers in immunology · 2016
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Leptospira interrogans binds to cadherins.PLoS neglected tropical diseases · 2014
    Article
  15. Characterization of three novel adhesins of Leptospira interrogans.The American journal of tropical medicine and hygiene · 2013
    Article
  16. Article
  17. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Renata Siqueira MendesCentro de Biotecnologia, Instituto Butantan, Avenida Vital Brazil, 1500, 05503-900, Sao Paulo, SP, Brazil.
Marina Von Atzingen
Zenaide Maria de Morais
Amane Paldes Gonçales
Solange M T Serrano
Amanda F Asega
Eliete Caló Romero
Silvio Arruda Vasconcellos
Ana Lucia Tabet O Nascimento
Instituto Butantan · BRFundação de Estudo e Pesquisa em Medicina Veterinária e Zootecnia · BRInstituto Adolfo Lutz · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Leptospirosis is an emerging infectious disease caused by pathogenic species of Leptospira. In this work, we report the cloning, expression, purification, and characterization of two predicted leptospiral outer membrane proteins, LIC11469 and LIC11030. The LIC11469 protein is well conserved among leptospiral strains, while LIC11030 was identified only in Leptospira interrogans. We confirmed by surface proteolysis of intact leptospires with proteinase K that these proteins are most likely new surface leptospiral proteins. The recombinant proteins were evaluated for their capacity to attach to extracellular matrix (ECM) components and to plasminogen. The leptospiral protein encoded by LIC11469, named Lsa20 (leptospiral surface adhesin of 20 kDa), binds to laminin and to plasminogen. The binding with both components was not detected when Lsa20 was previously denatured or blocked with anti-Lsa20 antibodies. Moreover, Lsa20 binding to laminin was also confirmed by surface plasmon resonance (SPR). Laminin competes with plasminogen for binding to Lsa20, suggesting the same ligand-binding site. Lsa20-bound plasminogen could be converted to enzymatically active plasmin, capable of cleaving plasmin substrate d-valyl-leucyl-lysine-p-nitroanilide dihydrochloride. Lsa20 was recognized by antibodies in confirmed-leptospirosis serum samples, suggesting that this protein is expressed during infection. Taken together, our results indicate that Lsa20 is a novel leptospiral adhesin that in concert with the host-derived plasmin may help the bacteria to adhere and to spread through the hosts.

Indexed as

Adhesins, BacterialBacterial AdhesionComputational BiologyGene Expression Regulation, BacterialHumansLamininLeptospira interrogansLeptospirosisMolecular BiologyMolecular Sequence DataPlasminogenProtein BindingRecombinant ProteinsAdhesins, BacterialLamininPlasminogenRecombinant Proteins

Identifiers

PMID21844229
PMCPMC3257903
OpenAlexW1983589480

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.